ID J3NDZ1_ORYBR Unreviewed; 849 AA.
AC J3NDZ1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=EF-hand domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB12G21990.1};
RN [1] {ECO:0000313|EnsemblPlants:OB12G21990.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB12G21990.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB12G21990.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC {ECO:0000256|ARBA:ARBA00007975}.
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DR AlphaFoldDB; J3NDZ1; -.
DR STRING; 4533.J3NDZ1; -.
DR EnsemblPlants; OB12G21990.1; OB12G21990.1; OB12G21990.
DR Gramene; OB12G21990.1; OB12G21990.1; OB12G21990.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_335989_0_0_1; -.
DR OMA; DWTTSFR; -.
DR Proteomes; UP000006038; Chromosome 12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013623; NADPH_Ox.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF61; OS12G0541300 PROTEIN; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08414; NADPH_Ox; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..176
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 500..601
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..675
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 96222 MW; DAF6355F94FEDE78 CRC64;
MASGNGGTPP AAADYRSSDS RSSSRRSTRF KEDNEYVEIT LDVKGDDTVA IQSIRNGGDL
PEFLNSSVVT NGWPEVEKRF DRLAVDGFLL RSRFGQCIGM VGSEEFAVQI FDALARRRGI
TAQLLTKDQV REFWEQLSDP GFDAKLQTFF DMVDKNADGQ ITEEELKEVL TLTASANKLS
KILERVDEYT ALIMEELDPD QLGYIDISNL EALLLLPPSQ APSKLVTHSS NISQLISQKL
VPTNDRNPLR RGLRKLGYFM EDNWKRVWVV ALWLAINAGL FTWKFMAYKR HPTFDVMGYC
VCVAKGGAET TKFNMALILL PVCRNTITWL RSRTKLDAAI PFNDNINFHK VVAGGVVVGV
ALHGVTHLTC DFPRLLHASD AVYEPMKKYF GQTRVPNYWW FVKGVEGITG VIMVVLMAIA
YTLAHPWFRR SKLSEGNPLK RLSGFNMFWY SHHLFVVVYI AFVVHGVCLY INRTWWKQTT
WMYLAIPLLL YAGERIFRAL RSHGFTTVRI EKVAIYPGNV IAIYMSKPPG FKYKSGQYIY
VNCGEVSPFE WHPFTITSAP GDSYLSMHIR CRGDWTSSFR AIFSQICRPP MNGQSGLLRA
DCMSMEHNAR RCRRCGWGGG CVAVVQVPEA ADRRAVRRAG AGLLEVRRAP PHRPRHRRHP
SHQHRQGRPQ PHPGRRRGPR LASGQPRQGR RRRLQGVHDG PGVLLLVHAG GRVVRVVPRR
DERGRRPRRR RADRAPQPLH QRVRGGGRPV GAGDDAAGAP PRQERRRRRL RHPGPHPLRP
PQLARRLQAP RRQPPGPARR RLLLRRPDPH AGAPPPRPGL LPQDHHQVRL PQGELLIHSR
PRSSQQKSP
//